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epmA EF-P-lysine lysyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948672, updated on 3-Dec-2024

Summary

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Official Symbol
epmA
Official Full Name
EF-P-lysine lysyltransferase
Primary source
ECOCYC:EG11211
Locus tag
b4155
See related
ASAP:ABE-0013610
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK4151; genX; poxA; yjeA
Summary
The poxA pleiotropic phenotypes are not due to a defect in pyruvate oxidase. [More information is available at EcoGene: EG11211]. PoxA is suggested to regulate pyruvate oxidase . [More information is available at EcoCyc: EG11211].
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Genomic context

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Sequence:
NC_000913.3 (4382643..4383620)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene fumarate reductase membrane protein FrdC Neighboring gene fumarate reductase iron-sulfur protein Neighboring gene fumarate reductase flavoprotein subunit Neighboring gene putative transporter YjeM Neighboring gene uncharacterized protein YjeN Neighboring gene DUF2645 domain-containing inner membrane protein YjeO

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. De-novo designed β-lysine derivatives can both augment and diminish the proliferation rates of E. coli through the action of Elongation Factor P. McDonnell CM, et al. Bioorg Med Chem Lett, 2022 Mar 1. PMID 35032607
  2. Evidence for a new Escherichia coli protein resembling a lysyl-tRNA synthetase. Kong L, et al. Gene, 1991 Dec 1. PMID 1761227
  3. Pleiotropic effects of poxA regulatory mutations of Escherichia coli and Salmonella typhimurium, mutations conferring sulfometuron methyl and alpha-ketobutyrate hypersensitivity. Van Dyk TK, et al. J Bacteriol, 1987 Oct. PMID 2820932, Free PMC Article
  4. Mapping nonselectable genes of Escherichia coli by using transposon Tn10: location of a gene affecting pyruvate oxidase. Chang YY, et al. J Bacteriol, 1982 Sep. PMID 6286595, Free PMC Article
  5. Molecular and functional characterization of Salmonella enterica serovar typhimurium poxA gene: effect on attenuation of virulence and protection. Kaniga K, et al. Infect Immun, 1998 Dec. PMID 9826331, Free PMC Article

See all (21) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. De-novo designed beta-lysine derivatives can both augment and diminish the proliferation rates of E. coli through the action of Elongation Factor P.
    Title: De-novo designed β-lysine derivatives can both augment and diminish the proliferation rates of E. coli through the action of Elongation Factor P.
  2. Synthetic post-translational modifications of elongation factor P using the ligase EpmA.
    Title: Synthetic post-translational modifications of elongation factor P using the ligase EpmA.
  3. GenX-elongation factor P-lysyl adenylate analogue crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a=105.93, b=102.96, c=119.94 A, beta=99.4 degrees, and diffracted to 2.5 A resolution
    Title: Crystallization and preliminary X-ray crystallographic study of GenX, a lysyl-tRNA synthetase paralogue from Escherichia coli, in complex with translation elongation factor P.
  4. reveal that the translation elongation factor P (EF-P) lysylation by GenX is enhanced by YjeK (lysine 2,3-aminomutase paralog)
    Title: A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P.
  5. Misacylation of yeast amber suppressor tRNA(Tyr) is via E. coli lysyl-tRNA synthetase.
    Title: Misacylation of yeast amber suppressor tRNA(Tyr) by E. coli lysyl-tRNA synthetase and its effective repression by genetic engineering of the tRNA sequence.
Submit: New GeneRIF Correction

General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables acid-ammonia (or amide) ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables lysine-tRNA ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables lysine-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein-lysine lysyltransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables tRNA binding IBA
Inferred from Biological aspect of Ancestor
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within cellular response to acidic pH IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in lysyl-tRNA aminoacylation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in lysyl-tRNA aminoacylation IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within post-translational protein modification RCA
inferred from Reviewed Computational Analysis
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
EF-P-lysine lysyltransferase

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    4382643..4383620
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418579.2 EF-P-lysine lysyltransferase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_418579.2

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A0H2Z5K9, A0A1X3J951, C3SGA2
    Conserved Domains (1) summary
    PRK09350
    Location:12 → 317
    PRK09350; elongation factor P--(R)-beta-lysine ligase
Nucleotide Protein
Heading Accession and Version

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